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Potassium in PDB 5uka: Salmonella Typhimurium Ahpc E49Q Mutant

Enzymatic activity of Salmonella Typhimurium Ahpc E49Q Mutant

All present enzymatic activity of Salmonella Typhimurium Ahpc E49Q Mutant:
1.11.1.15;

Protein crystallography data

The structure of Salmonella Typhimurium Ahpc E49Q Mutant, PDB code: 5uka was solved by A.Perkins, K.Nelson, D.Parsonage, L.Poole, P.A.Karplus, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.26 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 126.902, 171.950, 135.766, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / 21

Other elements in 5uka:

The structure of Salmonella Typhimurium Ahpc E49Q Mutant also contains other interesting chemical elements:

Chlorine (Cl) 5 atoms
Sodium (Na) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Salmonella Typhimurium Ahpc E49Q Mutant (pdb code 5uka). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the Salmonella Typhimurium Ahpc E49Q Mutant, PDB code: 5uka:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in 5uka

Go back to Potassium Binding Sites List in 5uka
Potassium binding site 1 out of 3 in the Salmonella Typhimurium Ahpc E49Q Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Salmonella Typhimurium Ahpc E49Q Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K202

b:67.0
occ:0.50
O A:HOH375 2.5 60.9 1.0
O A:THR72 3.1 36.1 1.0
O A:HOH313 3.5 50.3 1.0
HA A:ASP73 3.7 44.7 1.0
HB A:THR72 3.8 41.5 1.0
C A:THR72 3.9 34.3 1.0
OG1 A:THR72 4.0 35.7 1.0
CB A:THR72 4.4 34.5 1.0
HA A:PRO99 4.4 35.3 1.0
N A:ASP73 4.4 34.2 1.0
CA A:ASP73 4.5 37.2 1.0
HG1 A:THR72 4.7 42.9 1.0
O A:HOH308 4.7 44.5 1.0
CA A:THR72 4.8 35.4 1.0
HB3 A:PRO99 4.9 48.9 1.0
HD23 A:LEU116 5.0 47.4 1.0
O A:GLY115 5.0 39.2 1.0
OD1 A:ASP73 5.0 52.4 1.0

Potassium binding site 2 out of 3 in 5uka

Go back to Potassium Binding Sites List in 5uka
Potassium binding site 2 out of 3 in the Salmonella Typhimurium Ahpc E49Q Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Salmonella Typhimurium Ahpc E49Q Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K202

b:72.8
occ:1.00
O C:THR72 2.7 28.2 1.0
O B:HOH322 2.7 42.5 1.0
O C:HOH417 2.7 37.1 1.0
O B:THR72 3.0 31.5 1.0
O C:HOH484 3.1 48.5 1.0
O B:HOH359 3.1 43.0 1.0
HA C:PRO99 3.5 34.6 1.0
HA B:PRO99 3.6 35.0 1.0
HB C:THR72 3.6 33.7 1.0
C C:THR72 3.7 32.5 1.0
HA C:ASP73 3.7 37.2 1.0
HB B:THR72 3.8 33.7 1.0
HA B:ASP73 3.8 33.5 1.0
C B:THR72 3.9 34.4 1.0
HB3 B:PRO99 4.0 41.5 1.0
HB3 C:PRO99 4.0 33.9 1.0
OG1 C:THR72 4.2 30.1 1.0
CB C:THR72 4.3 28.1 1.0
CA C:PRO99 4.3 28.9 1.0
HG1 C:THR72 4.4 36.1 1.0
N C:ASP73 4.4 30.8 1.0
OG1 B:THR72 4.4 28.1 1.0
CB B:THR72 4.4 28.1 1.0
CA B:PRO99 4.4 29.1 1.0
O C:PRO99 4.4 29.4 1.0
CA C:ASP73 4.5 31.0 1.0
CB B:PRO99 4.5 34.6 1.0
O B:PRO99 4.5 27.0 1.0
CB C:PRO99 4.5 28.2 1.0
HB2 B:PRO99 4.5 41.5 1.0
N B:ASP73 4.6 28.4 1.0
CA B:ASP73 4.6 27.9 1.0
CA C:THR72 4.6 35.1 1.0
HB2 C:PRO99 4.7 33.9 1.0
CA B:THR72 4.8 29.9 1.0
C C:PRO99 4.9 28.4 1.0
O C:HOH505 5.0 52.1 1.0
O C:HOH402 5.0 40.7 1.0

Potassium binding site 3 out of 3 in 5uka

Go back to Potassium Binding Sites List in 5uka
Potassium binding site 3 out of 3 in the Salmonella Typhimurium Ahpc E49Q Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Salmonella Typhimurium Ahpc E49Q Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K202

b:99.8
occ:1.00
O E:THR72 2.7 51.4 1.0
O D:HOH353 2.8 64.7 1.0
O E:HOH324 2.9 72.5 1.0
O D:THR72 2.9 43.6 1.0
O E:HOH309 2.9 53.7 1.0
O D:HOH372 3.0 62.8 1.0
HA D:ASP73 3.3 58.5 1.0
HA E:ASP73 3.4 56.9 1.0
HA E:PRO99 3.7 61.4 1.0
C D:THR72 3.7 44.4 1.0
C E:THR72 3.7 52.6 1.0
HA D:PRO99 3.9 54.2 1.0
HB E:THR72 3.9 63.1 1.0
HB D:THR72 4.0 55.1 1.0
HB3 E:PRO99 4.1 60.2 1.0
CA D:ASP73 4.1 48.8 1.0
HB3 D:PRO99 4.2 54.4 1.0
N D:ASP73 4.2 43.6 1.0
CA E:ASP73 4.2 47.4 1.0
N E:ASP73 4.3 43.7 1.0
O E:HOH301 4.4 60.1 1.0
OG1 D:THR72 4.4 43.4 1.0
OG1 E:THR72 4.5 52.9 1.0
O D:HOH306 4.5 55.2 1.0
CA E:PRO99 4.5 51.1 1.0
CB D:THR72 4.5 45.9 1.0
CB E:THR72 4.5 52.6 1.0
HG1 E:THR72 4.6 63.5 1.0
HG23 E:THR74 4.7 61.3 1.0
CB E:PRO99 4.7 50.2 1.0
CA D:PRO99 4.7 45.2 1.0
CA D:THR72 4.8 44.9 1.0
C E:ASP73 4.8 48.4 1.0
CA E:THR72 4.8 46.6 1.0
CB D:PRO99 4.8 45.3 1.0
O E:PRO99 4.8 50.7 1.0
H E:THR74 4.8 57.9 1.0
HG23 D:THR74 4.9 58.2 1.0
H D:ASP73 4.9 52.3 1.0
C D:ASP73 4.9 47.2 1.0
HB2 E:PRO99 4.9 60.2 1.0
OD1 D:ASP73 4.9 60.0 1.0
H D:THR74 5.0 56.4 1.0
HB2 D:PRO99 5.0 54.4 1.0

Reference:

K.J.Nelson, A.Perkins, A.E.D.Van Swearingen, S.Hartman, A.E.Brereton, D.Parsonage, F.R.Salsbury Jr., P.A.Karplus, L.B.Poole. Experimentally Dissecting the Origins of Peroxiredoxin Catalysis. Antioxid.Redox Signal. V. 28 521 2018.
ISSN: ESSN 1557-7716
PubMed: 28375740
DOI: 10.1089/ARS.2016.6922
Page generated: Mon Dec 14 00:08:20 2020

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